一种结合HIV-1 Gag而非Gag衍生蛋白的单克隆抗体的表位作图。

Epitope mapping of a monoclonal antibody which binds HIV-1 Gag and not the Gag-derived proteins.

作者信息

Sarubbi E, Denaro M

机构信息

Lepetit Research Center, Marion Merrell Dow Research Institute, Gerenzano, VA, Italy.

出版信息

FEBS Lett. 1993 Dec 13;335(3):335-7. doi: 10.1016/0014-5793(93)80413-o.

DOI:10.1016/0014-5793(93)80413-o

PMID:7505237

Abstract

Monoclonal antibody (MAb) 1G12 binds the uncleaved HIV-1 Gag polypeptide (p55), but fails to recognize the final products of the proteolytic processing [Sarubbi, E. et al. (1991) FEBS Lett. 279, 265-269]. In this report we show that binding of MAb 1G12 to a 110-residue Gag fragment containing the p17-p24 cleavage site prevents proteolysis of this site by the HIV-1 protease. Competition studies with synthetic peptides have been performed to map the binding site of MAb 1G12 on Gag. The antibody recognizes a sequential epitope that spans the HIV-1 protease cleavage site; determinants located on both p17 and p24 are required for antibody binding. MAb 1G12 is also shown to lack any cross-reactivity with other HIV-1 protease cleavage sites.

摘要

单克隆抗体（MAb）1G12可结合未切割的HIV-1 Gag多肽（p55），但无法识别蛋白水解加工的最终产物[萨鲁比，E.等人（1991年）《欧洲生物化学学会联合会快报》279卷，第265 - 269页]。在本报告中，我们表明MAb 1G12与包含p17 - p24切割位点的110个氨基酸残基的Gag片段结合，可阻止HIV-1蛋白酶对该位点的蛋白水解。已进行了与合成肽的竞争研究，以绘制MAb 1G12在Gag上的结合位点。该抗体识别跨越HIV-1蛋白酶切割位点的连续表位；抗体结合需要位于p17和p24上的决定簇。还表明MAb 1G12与其他HIV-1蛋白酶切割位点无任何交叉反应。